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B1LNL9 (PFKA_ECOSM) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent 6-phosphofructokinase isozyme 1

Short name=ATP-PFK 1
Short name=Phosphofructokinase 1
EC=2.7.1.11
Alternative name(s):
6-phosphofructokinase isozyme I
Phosphohexokinase 1
Gene names
Name:pfkA
Ordered Locus Names:EcSMS35_4356
OrganismEscherichia coli (strain SMS-3-5 / SECEC) [Complete proteome] [HAMAP]
Taxonomic identifier439855 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length320 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis By similarity. HAMAP-Rule MF_00339

Catalytic activity

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. HAMAP-Rule MF_00339

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00339

Enzyme regulation

Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate By similarity. HAMAP-Rule MF_00339

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP-Rule MF_00339

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00339

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00339.

Sequence similarities

Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade "B1" sub-subfamily.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 320320ATP-dependent 6-phosphofructokinase isozyme 1 HAMAP-Rule MF_00339
PRO_1000120043

Regions

Nucleotide binding73 – 742ATP By similarity
Nucleotide binding103 – 1064ATP By similarity
Region22 – 265Allosteric activator ADP binding; shared with dimeric partner By similarity
Region55 – 606Allosteric activator ADP binding; shared with dimeric partner By similarity
Region126 – 1283Substrate binding By similarity
Region170 – 1723Substrate binding By similarity
Region186 – 1883Allosteric activator ADP binding By similarity
Region214 – 2163Allosteric activator ADP binding By similarity
Region250 – 2534Substrate binding By similarity

Sites

Active site1281Proton acceptor By similarity
Metal binding1041Magnesium; catalytic By similarity
Binding site121ATP; via amide nitrogen By similarity
Binding site1551Allosteric activator ADP By similarity
Binding site1631Substrate; shared with dimeric partner By similarity
Binding site2121Allosteric activator ADP By similarity
Binding site2231Substrate By similarity
Binding site2441Substrate; shared with dimeric partner By similarity

Sequences

Sequence LengthMass (Da)Tools
B1LNL9 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: D03D79F6A5536A41

FASTA32034,842
        10         20         30         40         50         60 
MIKKIGVLTS GGDAPGMNAA IRGVVRSALT EGLEVMGIYD GYLGLYEDRM VQLDRYSVSD 

        70         80         90        100        110        120 
MINRGGTFLG SARFPEFRDE NIRAVAIENL KKRGIDALVV IGGDGSYMGA MRLTEMGFPC 

       130        140        150        160        170        180 
IGLPGTIDND IKGTDYTIGF FTALSTVVEA IDRLRDTSSS HQRISVVEVM GRYCGDLTLA 

       190        200        210        220        230        240 
AAIAGGCEFV VVPEVEFSRE DLVNEIKAGI AKGKKHAIVA ITEHMCDVDE LAHFIEKETG 

       250        260        270        280        290        300 
RETRATVLGH IQRGGSPVPY DRILASRMGA YAIDLLLAGY GGRCVGIQNE QLVHHDIIDA 

       310        320 
IENMKRPFKG DWLDCAKKLY 

« Hide

References

[1]"Insights into the environmental resistance gene pool from the genome sequence of the multidrug-resistant environmental isolate Escherichia coli SMS-3-5."
Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C., Ravel J., Stepanauskas R.
J. Bacteriol. 190:6779-6794(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SMS-3-5 / SECEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000970 Genomic DNA. Translation: ACB16769.1.
RefSeqYP_001746301.1. NC_010498.1.

3D structure databases

ProteinModelPortalB1LNL9.
SMRB1LNL9. Positions 1-320.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING439855.EcSMS35_4356.

Proteomic databases

PRIDEB1LNL9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB16769; ACB16769; EcSMS35_4356.
GeneID6144511.
KEGGecm:EcSMS35_4356.
PATRIC18437634. VBIEscCol6161_4484.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000248870.
KOK00850.
OMAGFGGRCV.
OrthoDBEOG644ZRM.

Enzyme and pathway databases

BioCycECOL439855:GHHB-4350-MONOMER.
UniPathwayUPA00109; UER00182.

Family and domain databases

HAMAPMF_00339. Phosphofructokinase_I_B1.
InterProIPR012003. ATP_PFK_prok.
IPR012828. PFKA_ATP.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamPF00365. PFK. 1 hit.
[Graphical view]
PIRSFPIRSF000532. ATP_PFK_prok. 1 hit.
PRINTSPR00476. PHFRCTKINASE.
SUPFAMSSF53784. SSF53784. 1 hit.
TIGRFAMsTIGR02482. PFKA_ATP. 1 hit.
PROSITEPS00433. PHOSPHOFRUCTOKINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePFKA_ECOSM
AccessionPrimary (citable) accession number: B1LNL9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 29, 2008
Last modified: July 9, 2014
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways